1exp
From Proteopedia
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| - | [[Image:1exp.gif|left|200px]]<br /> | + | [[Image:1exp.gif|left|200px]]<br /><applet load="1exp" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1exp" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1exp, resolution 1.8Å" /> | caption="1exp, resolution 1.8Å" /> | ||
'''BETA-1,4-GLYCANASE CEX-CD'''<br /> | '''BETA-1,4-GLYCANASE CEX-CD'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EXP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cellulomonas_fimi Cellulomonas fimi]. | + | 1EXP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cellulomonas_fimi Cellulomonas fimi]. Known structural/functional Sites: <scene name='pdbsite=ABC:Acid Base Catalyst'>ABC</scene> and <scene name='pdbsite=NUC:Catalytic Nucleophile, Covalently Linked To The Fluoroce ...'>NUC</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EXP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: signal]] | [[Category: signal]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 15:13:58 2007'' |
Revision as of 13:04, 18 December 2007
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BETA-1,4-GLYCANASE CEX-CD
Overview
The three-dimensional structure of a catalytically competent, glycosyl-enzyme intermediate of a retaining beta-1,4-glycanase has been, determined at a resolution of 1.8 A by X-ray diffraction. A fluorinated, slow substrate forms an alpha-D-glycopyranosyl linkage to one of the two, invariant carboxylates, Glu 233, as supported in solution by 19F-NMR, studies. The resulting ester linkage is coplanar with the cyclic oxygen of, the proximal saccharide and is inferred to form a strong hydrogen bond, with the 2-hydroxyl of that saccharide unit in natural substrates. The, active-site architecture of this covalent intermediate gives insights into, both the classical double-displacement catalytic mechanism and the basis, for the enzyme's specificity.
About this Structure
1EXP is a Single protein structure of sequence from Cellulomonas fimi. Known structural/functional Sites: and . Full crystallographic information is available from OCA.
Reference
Crystallographic observation of a covalent catalytic intermediate in a beta-glycosidase., White A, Tull D, Johns K, Withers SG, Rose DR, Nat Struct Biol. 1996 Feb;3(2):149-54. PMID:8564541
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